Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.

Authors

Mary B. Sevigny, Department of Natural Sciences and Mathematics, Dominican University of CaliforniaFollow
Kamara Graham, Department of Natural Sciences and Mathematics,Dominican University of California
Esmeralda Ponce, Department of Natural Sciences and Mathematics, Dominican University of CaliforniaFollow
Maggie Louie, Department of Natural Sciences and Mathematics, Dominican University of CaliforniaFollow
Kylie Mitchell, Department of Natural Sciences and Mathematics, Dominican University of CaliforniaFollow

Department

Department of Natural Sciences and Mathematics

Document Type

Article

Source

Pharmacological Research

Publication Date

4-1-2012

ISSN

1096-1186

Volume

65

Issue

4

First Page

445

Last Page

450

Abstract

Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer. The rate-limiting step in the prostanoid biosynthesis pathway is catalyzed by cyclooxygenase-2 (COX-2). COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580). In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib. Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.

PubMed ID

22245433

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